Evidence map›Paper›PMID 24562855›Full record

ArticleJournal of molecular modeling2014

Homology modeling and virtual screening for antagonists of protease from yellow head virus.

Sasimanas Unajak, Orathai Sawatdichaikul, Napat Songtawee, Siriluk Rattanabunyong, Anchalee Tassnakajon, Nontawith Areechon, Ikuo Hirono, Hidehiro Kondo, Pongsak Khunrae, Triwit Rattanarojpong and 1 more

Open access · bronzeAbstract read
In one paragraph

Article in Journal of molecular modeling, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
0.4field-weighted citation impact, top 38% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

1 citing paper in PubMed, 11 citations in OpenAlex.

  1. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

11 authors at 5 institutions in 2 countries.

Sasimanas UnajakDepartment of Biochemistry, Faculty of Science, Kasetsart University, 50 Ngam Wong Wan Rd, Chatuchak, Bangkok, 10900, Thailand.
Orathai Sawatdichaikul
Napat Songtawee
Siriluk Rattanabunyong
Anchalee Tassnakajon
Nontawith Areechon
Ikuo Hirono
Hidehiro Kondo
Pongsak Khunrae
Triwit Rattanarojpong
Kiattawee Choowongkomon
Kasetsart University · THKing Mongkut's University of Technology Thonburi · THTokyo University of Marine Science and Technology · JPChulalongkorn University · THMahidol University · TH

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Yellow head virus (YHV) is one of the causative agents of shrimp viral disease. The prevention of YHV infection in shrimp has been developed by various methods, but it is still insufficient to protect the mass mortality in shrimp. New approaches for the antiviral drug development for viral infection have been focused on the inhibition of several potent viral enzymes, and thus the YHV protease is one of the interesting targets for developing antiviral drugs according to the pivotal roles of the enzyme in an early stage of viral propagation. In this study, a theoretical modeling of the YHV protease was constructed based on the folds of several known crystal structures of other viral proteases, and was subsequently used as a target for virtual screening-molecular docking against approximately 1364 NCI structurally diversity compounds. A complex between the protease and the hit compounds was investigated for intermolecular interactions by molecular dynamics simulations. Five best predicted compounds (NSC122819, NSC345647, NSC319990, NSC50650, and NSC5069) were tested against bacterial expressed YHV. The NSC122819 showed the best inhibitory characteristic among the candidates, while others showed more than 50 % of inhibition in the assay condition. These compounds could potentially be inhibitors for curing YHV infection.

Indexed as

Models, MolecularAmino Acid SequenceAnimalsAntiviral AgentsBinding SitesEnzyme InhibitorsHydrogen BondingMolecular Docking SimulationMolecular Dynamics SimulationMolecular Sequence DataMolecular StructurePenaeidaePeptide HydrolasesProtein BindingProtein Structure, TertiaryRoniviridaeAntiviral AgentsEnzyme InhibitorsPeptide HydrolasesViral Proteins

Identifiers

PMID24562855
PMCPMC7087857
OpenAlexW2040797574

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.